The characterization of a thermostable activator of beta-D-glucosidase in normal human saliva.
The existence of thermostable activators of beta-D-glucosidase (EC 3.2.1.21) in Gaucher tissues is known. We demonstrate the presence of a thermostable factor in normal human saliva which activates the beta-D-glucosidase of saliva. The activator is specific for beta-glucosidase. It is dialysable and susceptible to pronase digestion. Sephadex G-25 gel filtration indicates that the activator is of low molecular weight, and polyacrylamide gel electrophoresis shows the low molecular weight fraction to migrate as two closely moving protein bands. A major proportion of the activator does not bind to concanavalin A-Sepharose. The activator appears to act by binding to or modifying the salivary beta-glucosidase in a time-dependent manner.
D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004789:Enzyme Activation; D005260:Female; D005959:Glucosidases / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D011402:Pronase / Q000378:metabolism; D012463:Saliva / Q000032:analysis / Q000201:enzymology*; D001617:beta-Glucosidase / Q000378:metabolism*
D005959:Glucosidases; D001617:beta-Glucosidase; D011402:Pronase